ID A0A124JZ67_9SPHN Unreviewed; 799 AA.
AC A0A124JZ67;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN ORFNames=AQZ49_05705 {ECO:0000313|EMBL:KUR79473.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR79473.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR79473.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR79473.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|HAMAP-Rule:MF_01403};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623,
CC ECO:0000256|HAMAP-Rule:MF_01403}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUR79473.1}.
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DR EMBL; LLZQ01000005; KUR79473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124JZ67; -.
DR STRING; 1739113.AQZ49_05705; -.
DR Proteomes; UP000061032; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02011; TPP_PK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR HAMAP; MF_01403; Phosphoketolase; 1.
DR InterPro; IPR023962; Phosphoketolase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
DR InterPro; IPR018969; Xul5P/Fru6P_PKetolase_C.
DR InterPro; IPR019790; Xul5P/Fru6P_PKetolase_CS.
DR InterPro; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR InterPro; IPR019789; Xul5P/Fru6P_PKetolase_ThDP_BS.
DR PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR PANTHER; PTHR31273:SF0; PHOSPHOKETOLASE-RELATED; 1.
DR Pfam; PF03894; XFP; 1.
DR Pfam; PF09363; XFP_C; 1.
DR Pfam; PF09364; XFP_N; 1.
DR PIRSF; PIRSF017245; Phosphoketolase; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01403}.
FT DOMAIN 14..377
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 595..797
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 799 AA; 87667 MW; 310878F644584CBD CRC64;
MALRSTGLAT LDPVEAALID AWWRAANYLS VGQIYLYDNP LLRDPLTLDH VKPLVVGHWG
TTPGQTFIYA HLNRVIVSHD LDMIYIAGPG HGGPALVGAT YLEGSYSEVY PGISRDTAGL
KKLFTQFSFP GGISSHVAPT TPGSIHEGGE LGYSLSHAFG AAFDNPDLIV ACVIGDGEAE
TGPLATAWHS NKFLSARTDG AVLPILHLNG YKISNPTVLA RIDPADLENL LTGYGWAPLF
VEGDDPAVMH QTMARAMDTA IAAIRRIQDD ARKNPARWDE PSPMPRWPMI VLRSPKGWTG
PKAVDGVAIE GTFHAHQVPL QVDADRPGHV ALLEAWMRSY RPEALFDDLG RLLPEIAALA
PQGGRRMGAN PHANGGLLLR DLHLPDVHDH ACTVPAPGAI TASDMGILGT FLRDVVELNR
ASANFRLFGP DETVSNMLDA VFDVTNRQWE EAIITHDEFL APDGRVLDAM LSEHNCEGWL
EGYLLTGRHG IFASYEAFVR IIDSMASQHA KWLKVTAQLP WRKPIASLNL LLSSHVWQQD
HNGFTHQDPG FLDHILTKKP AIVRAFLPPD ANCLLAVIDH CLHSRHHINV VVAGKHAMPQ
WLTIDAAIAH CAQGIGIWKW ASNDGDADAD PDLVMAACGD TPTLEVLAAV TILRTHLPDL
RVRVINVVDL TTLHLANEHP HGLTDADYDA LFTRTRPVIF AFHGYPGLVQ RLTHARTNRT
LSVHGYQEEG TITTAFDIRV QNGIDRFHLV LDAIGHLPDL GSRGAWLAQT MRDKLAAHTR
YIDVHGRDMP EIRDWVWPQ
//